Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Regulation of the contents and volume of vacuoles in plant cells depends on the coordinated activities of transporters and channels located in the tonoplast (vacuolar membrane). The three major components of the tonoplast are two proton pumps, the vacuolar H+-ATPase (V-ATPase) and H+-pyrophosphatase (V-PPase), and aquaporins. The tertiary structure of the V-ATPase complex and properties of its subunits have been characterized by biochemical and genetic techniques. These studies and a comparison with the F-type ATPase have enabled estimation of the dynamics of V-ATPase activity during catalysis. V-PPase, a simple proton pump, has been identified and cloned from various plant species and other organisms, such as algae and phototrophic bacteria, and functional motifs of the enzyme have been determined. Aquaporin, serving as the water channel, is the most abundant protein in the tonoplast in most plants. A common molecular architecture of aquaporins in mammals and plants has been determined by two-dimensional crystallographic analysis. Furthermore, recent molecular biological studies have revealed several other types of tonoplast transporters, such as the Ca2+-ATPase, Ca2+/H+ antiporter and Na+/H+ antiporter. Many other transporters and channels in the tonoplast remain to be identified; their activities have already been detected. This review presents an overview of the field and discusses recent findings on the tonoplast protein components that have been identified and their physiological consequences.
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PMID:TONOPLAST TRANSPORTERS: Organization and Function. 1133 6

Aquaporin-2 (AQP-2) is the vasopressin-regulated water channel expressed in the apical membrane of principal cells in the collecting duct and is involved in the urinary concentrating mechanism. In the rat distal colon, vasopressin stimulates water absorption through an unknown mechanism. With the hypothesis that AQP-2 could contribute to this vasopressin effect, we studied its presence in rat colonic epithelium. We used RT-PCR, in situ hybridization, immunoblotting, and immunocytochemistry to probe for AQP-2 expression. An AQP-2 amplicon was obtained through RT-PCR of colon epithelium RNA, and in situ hybridization revealed AQP-2 mRNA in colonic crypts and, to a lesser extent, in surface absorptive epithelial cells. AQP-2 protein was localized to the apical membrane of surface absorptive epithelial cells, where it colocalized with H(+)-K(+)-ATPase but not with Na(+)-K(+)-ATPase. AQP-2 was absent from the small intestine, stomach, and liver. Water deprivation increased the hybridization signal and the protein level (assessed by Western blot analysis) for AQP-2 in distal colon. This was accompanied by increased p-chloromercuriphenylsulfonic acid-sensitive water absorption. These results indicate that AQP-2 is present in the rat distal colon, where it might be involved in a water-sparing mechanism. In addition, these results support the idea that AQP-2, and probably other aquaporins, are involved in water absorption in the colon.
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PMID:Aquaporin-2, a regulated water channel, is expressed in apical membranes of rat distal colon epithelium. 1151 98

The expression and localization of AQP6 were examined in rat kidneys. In the kidney compartments, the expression was more intense in the outer medulla than in the cortex or inner medulla, and was negative in the glomerulus. During development, the AQP6 mRNA expression in the kidney was not detected in the fetus, but was recognized at birth, increased gradually by 4 weeks of age, and was unchanged thereafter. In situ hybridization demonstrated significant signals for AQP6 mRNA along the outer and inner medullary collecting ducts. Since the localization of the AQP6 mRNA-expressing cells was comparable to that of immunoreactive H+ ATPase-bearing cells in the collecting duct, they were identified as intercalated cells. No AQP6 mRNA signals were recognizable in other cells in the kidneys, including glomerular cells. No glomerular expression of AQP6 mRNA was confirmed by RT-PCR using total RNA extracted from the glomeruli. Immunohistochemistry using an antibody raised against recombinant rat AQP6 protein could localize the immunoreactivity in a population of collecting duct cells. Serial section observations indicated that the AQP6-immunoreactive cells corresponded to H+ ATPase bearing intercalated cells.
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PMID:Expression and immunolocalization of AQP6 in intercalated cells of the rat kidney collecting duct. 1157 29

The exact distributions of the different salt transport systems along the human cortical distal nephron are unknown. Immunohistochemistry was performed on serial cryostat sections of healthy parts of tumor nephrectomized human kidneys to study the distributions in the distal convolution of the thiazide-sensitive Na-Cl cotransporter (NCC), the beta subunit of the amiloride-sensitive epithelial Na channel (ENaC), the vasopressin-sensitive water channel aquaporin 2 (AQP2), and aquaporin 3 (AQP3), the H(+) ATPase, the Na-Ca exchanger (NCX), plasma membrane calcium-ATPase, and calbindin-D28k (CaBP). The entire human distal convolution and the cortical collecting duct (CCD) display calbindin-D28k, although in variable amounts. Approximately 30% of the distal convolution profiles reveal NCC, characterizing the distal convoluted tubule. NCC overlaps with ENaC in a short portion at the end of the distal convoluted tubule. ENaC is displayed all along the connecting tubule (70% of the distal convolution) and the CCD. The major part of the connecting tubule and the CCD coexpress aquaporin 2 with ENaC. Intercalated cells, undetected in the first 20% of the distal convolution, were interspersed among the segment-specific cells of the remainder of the distal convolution, and of the CCD. The basolateral calcium extruding proteins, Na-Ca exchanger (NCX), and the plasma membrane Ca(2+)-ATPase were found all along the distal convolution, and, in contrast to other species, along the CCD, although in varying amounts. The knowledge regarding the precise distribution patterns of transport proteins in the human distal nephron and the knowledge regarding the differences from that in laboratory animals may be helpful for diagnostic purposes and may also help refine the therapeutic management of electrolyte disorders.
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PMID:Human cortical distal nephron: distribution of electrolyte and water transport pathways. 1191 42

The expression of a putative water channel protein, aquaporin 3 (AQP-3), has been localised within branchial and intestinal tissues from the 'silver' life stage of the European eel Anguilla anguilla, using a specific polyclonal antibody directed against the C-terminal of the amino acid sequence. Western blots using the AQP-3 antiserum identified the presence of a major immunoreactive protein of 24 kDa in extracts of gills from both freshwater (FW) and 3 week seawater (SW)-acclimated eels. SW acclimation induced a 65 % reduction in AQP-3 protein abundance in the gill extracts. AQP-3 immunoreactivity was apparent throughout the branchial epithelium from both FW and SW-acclimated fish, but especially so within the chloride cells, which also stained heavily with specific antisera for the beta-subunit of the Na, K-ATPase. AQP-3 immunoreactivity not only colocalised with Na, K-ATPase within the basolateral tubular network but also stained the apical regions of the chloride cell where Na, K-ATPase was absent. Although there were no obvious differences in expression between the chloride cells of FW and SW-acclimated fish, considerably higher intensities of immunoreactivity were apparent near the periphery of the non-chloride cells of FW fish, especially within cells forming the base of the primary filaments and the branchial arch. AQP-3 immunoreactivity was also detected in intra-epithelial macrophage-like cells within the intestine of FW and SW-acclimated eels and in the mucous cells of the rectal epithelium of SW-acclimated fish. These results suggest that AQP-3 may play an important functional role in osmoregulation the teleostean gill but is unlikely to be responsible for the increases in intestinal water absorption that occur following SW acclimation.
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PMID:Immunolocalisation of aquaporin 3 in the gill and the gastrointestinal tract of the European eel Anguilla anguilla (L.). 1215 71

The rotor stoichiometry of F-ATPases has been revealed by the combined approaches of X-ray diffraction (XRD), electron crystallography, and atomic force microscopy (AFM). XRD showed the rotor from the yeast mitochondrial F-ATPase to contain 10 subunits. AFM was used to visualize the tetradecameric chloroplast rotors, and electron crystallography and AFM together revealed the rotors from Ilyobacter tartaricus to be composed of 11 subunits. While biochemical methods had determined an approximate stoichiometric value, precise measurements and new insights into a species-dependent rotor stoichiometry became available by applying the three structural tools together. The structures of AQP1, a water channel, and G1pF, a glycerol channel, were determined by electron crystallography and XRD. The combination of both of these structural tools with molecular dynamics simulations gave a differentiated description of the mechanisms determining the selectivity of water and glycerol channels. This illustrates that the combination of different methods in structural biology reveals more than each method alone.
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PMID:Assessing the structure of membrane proteins: combining different methods gives the full picture. 1244 Jun 97

Membrane-cytoskeleton interactions have been shown to be crucial to modulate polarity, cell shape and the paracellular pathway in epithelial MDCK cell monolayers. In particular, actin organization and myosin-dependent contractility play an important role in the regulation of these functions. Participation of myosin in vectorial transport, expressed as formation of domes, was investigated in confluent monolayers of high transepithelial electrical resistance (TER) plated on non-permeable supports. Cells exposed to 2,3-butanedione monoxime, a selective inhibitor of myosin ATPase, showed a remarkable increase in the number of domes. Replacement of extracellular Na+ and Cl- and inhibition of Na+-K+-ATPase blocked the induction of domes. The monoxime also caused a reduction of the TER leading to an increase in the paracellular flux of small molecular weight dextran. However, immunofluorescence microscopy of drug-treated cells showed that the localization and staining pattern of tight junction proteins ZO-1, occludin, and claudin 1, or the actin-myosin ring at the zonula adherens, were not modified. Treatment with the drug produced striking re-arrangements of actin filaments at the microvilli and at the basal level of the cells. Our data show that disruption of actin-myosin interaction at several cellular sites contributed importantly to the increased transport activity and the formation of the domes. These results point to the relevant role or actin-myosin dynamics and actin organization in the regulation of ion and water channel activity in these cells.
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PMID:2,3-butanedione monoxime (BDM), a potent inhibitor of actin-myosin interaction, induces ion and fluid transport in MDCK monolayers. 1250 Sep 2

Preimplantation development encompasses the interval from insemination until embryo implantation and thus includes the 'freeliving' period of oviduct and uterine development. Formation of the blastocyst is required for implantation and establishment of pregnancy, and is a principal determinant of embryo quality prior to embryo transfer. Development through this period is regulated by the expression of specific gene families that encode for cell polarity, cell junctional, cytoskeletal, ion transporter, and water channel gene products that direct the acquisition of cell polarity and differentiation of the outer cells of the early embryo. This results in the formation of the trophectoderm, which is the first epithelium of development. This review considers the roles of each of these gene families in trophectoderm differentiation and blastocyst formation. The principal hypothesis under investigation is that blastocyst formation is regulated by a Na/K-ATPase-generated trans-trophectoderm ion gradient that promotes the accumulation of water across the epithelium. This, combined with the formation of the tight junction seal controlling paracellular movement of water between adjacent trophectoderm cells, results in the formation of a fluid-filled blastocyst cavity and the expansion of the blastocyst. Results from recent experiments, however, have cast some doubt on the role of Na/K-ATPase in mediating these events and have defined water channels or Aquaporins (AQPs) as physiological mediators of fluid movement across the trophectoderm. In addition, studies have now implicated mitogen-activated protein kinase (MAPK) signaling as an important mediator of development to the blastocyst stage. Such studies define the physiology of blastocyst formation and serve to support the application of assisted reproductive technologies (ART) to both human and animal species.
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PMID:Molecular regulation of blastocyst formation. 1527 81

Molecular and pathogenetic mechanisms in sodium retention and water reabsorption of nephrotic edema are discussed. Are reported and analyzed molecular mechanisms about sodium retention in collecting duct cells regarding activation and surface expression of epithelial sodium channels (ENaC) and sodium-potassium-ATPase (Na,K-ATPase) by aldosterone, vasopressin, natriuretic peptide system (underfill theory): is necessary a better understanding about the dysregulation of ENaC and Na,K-ATPase surface expression and the resistance to natriuretic peptide system. Are also reported and analyzed molecular mechanisms of sodium retention in proximal tubule cells regarding intrinsic albumin toxicity upon type 3 sodium-hydrogen exchanger ionic pump and the activity of sodium-hydrogen exchanger regulatory factor protein (overfill theory): a better knowledge about the link between albumin, sodium-hydrogen exchanger type 3 (NHE3) ionic pump, sodium-hydrogen exchanger regulatory factor protein is necessary. Then molecular mechanisms of vasopressin free water retention through acquaporin water channels in collecting duct cells are discussed: further studies are necessary to understand vasopressin release pathway (osmotic/nonosmotic) and V2 receptor activation with cell surface expression of renal acquaporins water channel.
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PMID:Molecular pathogenetic mechanisms of nephrotic edema: progress in understanding. 1589 43

The choroid plexus epithelium secretes electrolytes and fluid in the brain ventricular lumen at high rates. Several channels and ion carriers have been identified as likely mediators of this transport in rodent choroid plexus. This study aimed to map several of these proteins to the human choroid plexus. Immunoperoxidase-histochemistry was employed to determine the cellular and subcellular localization of the proteins. The water channel, aquaporin (AQP) 1, was predominantly situated in the apical plasma membrane domain, although distinct basolateral and endothelial immunoreactivity was also observed. The Na(+)-K(+)-ATPase alpha(1)-subunit was exclusively localized apically in the human choroid plexus epithelial cells. Immunoreactivity for the Na(+)-K(+)-2Cl(-) cotransporter, NKCC1, was likewise confined to the apical plasma membrane domain of the epithelium. The Cl(-)/HCO(3)(-) exchanger, AE2, was localized basolaterally, as was the Na(+)-dependent Cl(-)/HCO(3)(-) exchanger, NCBE, and the electroneutral Na(+)-HCO(3)(-) cotransporter, NBCn1. No immunoreactivity was found toward the Na(+)-dependent acid/base transporters NHE1 or NBCe2. Hence, the human choroid plexus epithelium displays an almost identical distribution pattern of water channels and Na(+) transporters as the rat and mouse choroid plexus. This general cross species pattern suggests central roles for these transporters in choroid plexus functions such as cerebrospinal fluid production.
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PMID:Distribution of sodium transporters and aquaporin-1 in the human choroid plexus. 1648 71


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